EC |
1.1.1.234 |
Accepted name: |
flavanone 4-reductase |
Reaction: |
(2S)-flavan-4-ol + NADP+ = (2S)-flavanone + NADPH + H+ |
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For diagram of the biosynthesis of naringenin derivatives, click here |
Systematic name: |
(2S)-flavan-4-ol:NADP+ 4-oxidoreductase |
Comments: |
Involved in the biosynthesis of 3-deoxyanthocyanidins from flavanones such as naringenin or eriodictyol. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 115232-53-6 |
References: |
1. |
Stich, K. and Forkmann, G. Biosynthesis of 3-deoxyanthocyanins with flower extracts from Sinningia cardinalis. Phytochemistry 27 (1988) 785–789. |
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[EC 1.1.1.234 created 1992] |
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EC |
1.14.11.9 |
Accepted name: |
flavanone 3-dioxygenase |
Reaction: |
a (2S)-flavan-4-one + 2-oxoglutarate + O2 = a (2R,3R)-dihydroflavonol + succinate + CO2 |
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For diagram of flavonoid biosynthesis, click here and for diagram of naringenin derivatives biosynthesis, click here |
Other name(s): |
naringenin 3-hydroxylase; flavanone 3-hydroxylase; flavanone 3β-hydroxylase; flavanone synthase I; (2S)-flavanone 3-hydroxylase; naringenin,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating); F3H; flavanone,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating) |
Systematic name: |
(2S)-flavan-4-one,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating) |
Comments: |
Requires Fe2+ and ascorbate. This plant enzyme catalyses an early step in the flavonoid biosynthesis pathway, leading to the production of flavanols and anthocyanins. Substrates include (2S)-naringenin, (2S)-eriodictyol, (2S)-dihydrotricetin and (2S)-pinocembrin. Some enzymes are bifuctional and also catalyse EC 1.14.20.6, flavonol synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 75991-43-4 |
References: |
1. |
Forkmann, G., Heller, W. and Grisebach, H. Anthocyanin biosynthesis in flowers of Matthiola incana flavanone 3- and flavonoid 3′-hydroxylases. Z. Naturforsch. C: Biosci. 35 (1980) 691–695. |
2. |
Charrier, B., Coronado, C., Kondorosi, A. and Ratet, P. Molecular characterization and expression of alfalfa (Medicago sativa L.) flavanone-3-hydroxylase and dihydroflavonol-4-reductase encoding genes. Plant Mol. Biol. 29 (1995) 773–786. [PMID: 8541503] |
3. |
Pelletier, M.K. and Shirley, B.W. Analysis of flavanone 3-hydroxylase in Arabidopsis seedlings. Coordinate regulation with chalcone synthase and chalcone isomerase. Plant Physiol. 111 (1996) 339–345. [PMID: 8685272] |
4. |
Wellmann, F., Matern, U. and Lukačin, R. Significance of C-terminal sequence elements for Petunia flavanone 3β-hydroxylase activity. FEBS Lett. 561 (2004) 149–154. [DOI] [PMID: 15013767] |
5. |
Jin, Z., Grotewold, E., Qu, W., Fu, G. and Zhao, D. Cloning and characterization of a flavanone 3-hydroxylase gene from Saussurea medusa. DNA Seq 16 (2005) 121–129. [DOI] [PMID: 16147863] |
6. |
Shen, G., Pang, Y., Wu, W., Deng, Z., Zhao, L., Cao, Y., Sun, X. and Tang, K. Cloning and characterization of a flavanone 3-hydroxylase gene from Ginkgo biloba. Biosci Rep 26 (2006) 19–29. [DOI] [PMID: 16779664] |
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[EC 1.14.11.9 created 1983, modified 1989, modified 2004, modified 2016] |
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EC
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1.14.11.22
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Transferred entry: | flavone synthase. Now EC 1.14.20.5, flavone synthase
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[EC 1.14.11.22 created 2004, deleted 2018] |
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EC
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1.14.11.23
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Transferred entry: | flavonol synthase. Now EC 1.14.20.6, flavonol synthase
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[EC 1.14.11.23 created 2004, deleted 2018] |
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EC
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1.14.13.21
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Transferred entry: | flavonoid 3′-monooxygenase. Now EC 1.14.14.82, flavonoid 3′-monooxygenase.
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[EC 1.14.13.21 created 1983, deleted 2018] |
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EC
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1.14.13.88
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Transferred entry: | flavanoid 3,5-hydroxylase. Now EC 1.14.14.81, flavanoid 3,5-hydroxylase
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[EC 1.14.13.88 created 2004, deleted 2018] |
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EC
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1.14.13.103
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Transferred entry: | 8-dimethylallylnaringenin 2-hydroxylase. Now EC 1.14.14.142, 8-dimethylallylnaringenin 2-hydroxylase
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[EC 1.14.13.103 created 2007, deleted 2018] |
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EC
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1.14.13.136
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Transferred entry: | 2-hydroxyisoflavanone synthase. Now EC 1.14.14.87, 2-hydroxyisoflavanone synthase
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[EC 1.14.13.136 created 2011, modified 2013, deleted 2018] |
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EC
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1.14.13.152
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Transferred entry: | geraniol 8-hydroxylase. Now EC 1.14.14.83, geraniol 8-hydroxylase
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[EC 1.14.13.152 created 2012, deleted 2018] |
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EC |
1.14.14.81 |
Accepted name: |
flavanoid 3′,5′-hydroxylase |
Reaction: |
a flavanone + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = a 3′,5′-dihydroxyflavanone + 2 [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction) (1a) a flavanone + [reduced NADPH—hemoprotein reductase] + O2 = a 3′-hydroxyflavanone + [oxidized NADPH—hemoprotein reductase] + H2O (1b) a 3′-hydroxyflavanone + [reduced NADPH—hemoprotein reductase] + O2 = a 3′,5′-dihydroxyflavanone + [oxidized NADPH—hemoprotein reductase] + H2O |
|
For diagram of myricetin biosynthesis, click here, for diagram of the biosynthesis of naringenin derivatives, click here and for diagram of flavonoid biosynthesis, click here |
Other name(s): |
flavonoid 3′,5′-hydroxylase |
Systematic name: |
flavanone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3′,5′-dihydroxylating) |
Comments: |
A cytochrome P-450 (heme-thiolate) protein found in plants. The 3′,5′-dihydroxyflavanone is formed via the 3′-hydroxyflavanone. In Petunia hybrida the enzyme acts on naringenin, eriodictyol, dihydroquercetin (taxifolin) and dihydrokaempferol (aromadendrin). The enzyme catalyses the hydroxylation of 5,7,4′-trihydroxyflavanone (naringenin) at either the 3′ position to form eriodictyol or at both the 3′ and 5′ positions to form 5,7,3′,4′,5′-pentahydroxyflavanone (dihydrotricetin). The enzyme also catalyses the hydroxylation of 3,5,7,3′,4′-pentahydroxyflavanone (taxifolin) at the 5′ position, forming ampelopsin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 94047-23-1 |
References: |
1. |
Menting, J., Scopes, R.K. and Stevenson, T.W. Characterization of flavonoid 3′,5′-hydroxylase in microsomal membrane fraction of Petunia hybrida flowers. Plant Physiol. 106 (1994) 633–642. [PMID: 12232356] |
2. |
Shimada, Y., Nakano-Shimada, R., Ohbayashi, M., Okinaka, Y., Kiyokawa, S. and Kikuchi, Y. Expression of chimeric P450 genes encoding flavonoid-3′, 5′-hydroxylase in transgenic tobacco and petunia plants1. FEBS Lett. 461 (1999) 241–245. [DOI] [PMID: 10567704] |
3. |
de Vetten, N., ter Horst, J., van Schaik, H.P., de Boer, A., Mol, J. and Koes, R. A cytochrome b5 is required for full activity of flavonoid 3′, 5′-hydroxylase, a cytochrome P450 involved in the formation of blue flower colors. Proc. Natl. Acad. Sci. USA 96 (1999) 778–783. [DOI] [PMID: 9892710] |
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[EC 1.14.14.81 created 2004 as EC 1.14.13.88, transferred 2018 to EC 1.14.14.81] |
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EC |
1.14.14.82 |
Accepted name: |
flavonoid 3′-monooxygenase |
Reaction: |
a flavonoid + [reduced NADPH—hemoprotein reductase] + O2 = a 3′-hydroxyflavonoid + [oxidized NADPH—hemoprotein reductase] + H2O |
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For diagram of flavonoid biosynthesis, click here and for diagram of the biosynthesis of naringenin derivatives, click here |
Other name(s): |
CYP75B1 (gene name); flavonoid 3′-hydroxylase; flavonoid 3-hydroxylase (incorrect); NADPH:flavonoid-3′-hydroxylase (incorrect); flavonoid 3-monooxygenase (incorrect) |
Systematic name: |
flavonoid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3′-hydroxylating) |
Comments: |
A cytochrome P-450 (heme-thiolate) protein found in plants. Acts on a number of flavonoids, including the flavanone naringenin and the flavone apigenin. Does not act on 4-coumarate or 4-coumaroyl-CoA. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 75991-44-5 |
References: |
1. |
Forkmann, G., Heller, W. and Grisebach, H. Anthocyanin biosynthesis in flowers of Matthiola incana flavanone 3- and flavonoid 3′-hydroxylases. Z. Naturforsch. C: Biosci. 35 (1980) 691–695. |
2. |
Brugliera, F., Barri-Rewell, G., Holton, T.A. and Mason, J.G. Isolation and characterization of a flavonoid 3′-hydroxylase cDNA clone corresponding to the Ht1 locus of Petunia hybrida. Plant J. 19 (1999) 441–451. [PMID: 10504566] |
3. |
Schoenbohm, C., Martens, S., Eder, C., Forkmann, G. and Weisshaar, B. Identification of the Arabidopsis thaliana flavonoid 3′-hydroxylase gene and functional expression of the encoded P450 enzyme. Biol. Chem. 381 (2000) 749–753. [PMID: 11030432] |
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[EC 1.14.14.82 created 1983 as EC 1.14.13.21, transferred 2018 to EC 1.14.14.82] |
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EC |
1.14.14.83 |
Accepted name: |
geraniol 8-hydroxylase |
Reaction: |
geraniol + [reduced NADPH—hemoprotein reductase] + O2 = (6E)-8-hydroxygeraniol + [oxidized NADPH—hemoprotein reductase] + H2O |
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For diagram of acyclic monoterpenoid biosynthesis, click here |
Other name(s): |
CYP76B6 (gene name); G10H (gene name) |
Systematic name: |
geraniol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (8-hydroxylating) |
Comments: |
A cytochrome P-450 (heme thiolate) protein found in plants. Also hydroxylates nerol and citronellol, cf. EC 1.14.14.84, linalool 8-monooxygenase. The recommended numbering of geraniol gives 8-hydroxygeraniol as the product rather than 10-hydroxygeraniol as used by references 1-3. See prenol nomenclature Pr-1. The cloned enzyme also catalysed, but less efficiently, the 3′-hydroxylation of naringenin (cf. EC 1.14.14.82, flavonoid 3′-monooxygenase) [3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Collu, G., Unver, N., Peltenburg-Looman, A.M., van der Heijden, R., Verpoorte, R. and Memelink, J. Geraniol 10-hydroxylase, a cytochrome P450 enzyme involved in terpenoid indole alkaloid biosynthesis. FEBS Lett. 508 (2001) 215–220. [DOI] [PMID: 11718718] |
2. |
Wang, J., Liu, Y., Cai, Y., Zhang, F., Xia, G. and Xiang, F. Cloning and functional analysis of geraniol 10-hydroxylase, a cytochrome P450 from Swertia mussotii Franch. Biosci. Biotechnol. Biochem. 74 (2010) 1583–1590. [PMID: 20699579] |
3. |
Sung, P.H., Huang, F.C., Do, Y.Y. and Huang, P.L. Functional expression of geraniol 10-hydroxylase reveals its dual function in the biosynthesis of terpenoid and phenylpropanoid. J. Agric. Food Chem. 59 (2011) 4637–4643. [DOI] [PMID: 21504162] |
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[EC 1.14.14.83 created 2012 as EC 1.14.13.152, transferred 2018 to EC 1.14.14.83] |
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EC |
1.14.14.87 |
Accepted name: |
2-hydroxyisoflavanone synthase |
Reaction: |
(1) liquiritigenin + O2 + [reduced NADPH—hemoprotein reductase] = 2,4′,7-trihydroxyisoflavanone + H2O + [oxidized NADPH—hemoprotein reductase] (2) (2S)-naringenin + O2 + [reduced NADPH—hemoprotein reductase] = 2,4′,5,7-tetrahydroxyisoflavanone + H2O + [oxidized NADPH—hemoprotein reductase] |
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For diagram of daidzein biosynthesis, click here |
Glossary: |
liquiritigenin = 4′,7-dihydroxyflavanone
(2S)-naringenin = 4′,5,7-dihydroxyflavanone
2,4′,5,7-tetrahydroxyisoflavanone = 2-hydroxy-2,3-dihydrogenistein |
Other name(s): |
CYP93C; IFS; isoflavonoid synthase |
Systematic name: |
liquiritigenin, [reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (hydroxylating, aryl migration) |
Comments: |
A cytochrome P-450 (heme thiolate) protein found in plants. The reaction involves the migration of the 2-phenyl group of the flavanone to the 3-position of the isoflavanone. The 2-hydroxyl group is derived from the oxygen molecule. EC 4.2.1.105, 2-hydroxyisoflavanone dehydratase, acts on the products with loss of water and formation of genistein and daidzein, respectively. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Kochs, G. and Grisebach, H. Enzymic synthesis of isoflavones. Eur. J. Biochem. 155 (1986) 311–318. [DOI] [PMID: 3956488] |
2. |
Hashim, M.F., Hakamatsuka, T., Ebizuka, Y. and Sankawa, U. Reaction mechanism of oxidative rearrangement of flavanone in isoflavone biosynthesis. FEBS Lett. 271 (1990) 219–222. [DOI] [PMID: 2226805] |
3. |
Steele, C. L., Gijzen, M., Qutob, D. and Dixon, R.A. Molecular characterization of the enzyme catalyzing the aryl migration reaction of isoflavonoid biosynthesis in soybean. Arch. Biochem. Biophys. 367 (1999) 146–150. [DOI] [PMID: 10375412] |
4. |
Sawada, Y., Kinoshita, K., Akashi, T., Aoki, T. and Ayabe, S. Key amino acid residues required for aryl migration catalysed by the cytochrome P450 2-hydroxyisoflavanone synthase. Plant J. 31 (2002) 555–564. [DOI] [PMID: 12207646] |
5. |
Sawada, Y. and Ayabe, S. Multiple mutagenesis of P450 isoflavonoid synthase reveals a key active-site residue. Biochem. Biophys. Res. Commun. 330 (2005) 907–913. [DOI] [PMID: 15809082] |
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[EC 1.14.14.87 created 2011 as EC 1.14.13.136, modified 2013, transferred 2018 to EC 1.14.14.87] |
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EC |
1.14.14.142 |
Accepted name: |
8-dimethylallylnaringenin 2′-hydroxylase |
Reaction: |
sophoraflavanone B + [reduced NADPH—hemoprotein reductase] + O2 = leachianone G + [oxidized NADPH—hemoprotein reductase] + H2O |
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For diagram of sophoraflavanone G biosynthesis, click here |
Glossary: |
dimethylallyl = prenyl = 3-methylbut-2-en-1-yl
lavandulyl = 5-methyl-2-(prop-1-en-2-yl)hex-4-en-1-yl
leachianone G = (–)-(2S)-2′-hydroxy-8-prenylnaringenin = (–)-(2S)-2-(2,4-dihydroxyphenyl)-5,7-dihydroxy-8-(3-methylbut-2-en-1-yl)-2,3-dihydro-4H-chromen-4-one
naringenin = 5,7-dihydroxy-2-(4-hydroxyphenyl)-2,3-dihydrochromen-4-one
sophoraflavanone B = (–)-(2S)-8-prenylnaringenin = (–)-(2S)-5,7-dihydroxy-2-(4-hydroxyphenyl)-8-(3-methylbut-2-en-1-yl)-2,3-dihydro-4H-chromen-4-one |
Other name(s): |
8-DMAN 2′-hydroxylase |
Systematic name: |
sophoraflavanone-B,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (2′-hydroxylating) |
Comments: |
A membrane-bound cytochrome P-450 (heme-thiolate) protein that is associated with the endoplasmic reticulum [1,2]. This enzyme is specific for sophoraflavanone B as substrate. Along with EC 2.5.1.70 (naringenin 8-dimethylallyltransferase) and EC 2.5.1.71 (leachianone G 2′′-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone G biosynthetic pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Yamamoto, H., Yatou, A. and Inoue, K. 8-Dimethylallylnaringenin 2′-hydroxylase, the crucial cytochrome P450 mono-oxygenase for lavandulylated flavanone formation in Sophora flavescens cultured cells. Phytochemistry 58 (2001) 671–676. [DOI] [PMID: 11672730] |
2. |
Zhao, P., Inoue, K., Kouno, I. and Yamamoto, H. Characterization of leachianone G 2′′-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures. Plant Physiol. 133 (2003) 1306–1313. [DOI] [PMID: 14551337] |
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[EC 1.14.14.142 created 2007 asEC 1.14.13.103, transferred 2018 to EC 1.14.14.142] |
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EC |
1.14.14.162 |
Accepted name: |
flavanone 2-hydroxylase |
Reaction: |
a flavanone + [reduced NADPH—hemoprotein reductase] + O2 = a 2-hydroxyflavanone + [oxidized NADPH—hemoprotein reductase] + H2O |
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For diagram of licodione biosynthesis, click here |
Other name(s): |
CYP93G2 (gene name); CYP93B1 (gene name); (2S)-flavanone 2-hydroxylase; licodione synthase |
Systematic name: |
flavanone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (2-hydroxylating) |
Comments: |
A cytochrome P-450 (heme thiolate) plant enzyme that catalyses the 2-hydroxylation of multiple flavanones such as (2S)-naringenin, (2S)-eriodictyol, (2S)-pinocembrin, and (2S)-liquiritigenin. The products are meta-stable and exist in an equilibrium with open forms such as 1-(4-hydroxyphenyl)-3-(2,4,6-trihydroxyphenyl)propane-1,3-dione. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Otani, K., Takahashi, T., Furuya, T. and Ayabe, S. Licodione synthase, a cytochrome P450 monooxygenase catalyzing 2-hydroxylation of 5-deoxyflavanone, in cultured Glycyrrhiza echinata L. cells. Plant Physiol. 105 (1994) 1427–1432. [PMID: 12232298] |
2. |
Akashi, T., Aoki, T. and Ayabe, S. Identification of a cytochrome P450 cDNA encoding (2S)-flavanone 2-hydroxylase of licorice (Glycyrrhiza echinata L.; Fabaceae) which represents licodione synthase and flavone synthase II. FEBS Lett. 431 (1998) 287–290. [DOI] [PMID: 9708921] |
3. |
Du, Y., Chu, H., Chu, I.K. and Lo, C. CYP93G2 is a flavanone 2-hydroxylase required for C-glycosylflavone biosynthesis in rice. Plant Physiol. 154 (2010) 324–333. [PMID: 20647377] |
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[EC 1.14.14.162 created 2018. EC 1.14.14.140 created 2004 as EC 1.14.13.87, transferred 2018 to EC 1.14.14.140, transferred 2018 to EC 1.14.14.162] |
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EC |
1.14.20.5 |
Accepted name: |
flavone synthase I |
Reaction: |
a flavanone + 2-oxoglutarate + O2 = a flavone + succinate + CO2 + H2O |
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For diagram of flavonoid biosynthesis, click here and for diagram of the biosynthesis of naringenin derivatives, click here |
Other name(s): |
FNSI (gene name) |
Systematic name: |
flavanone,2-oxoglutarate:oxygen oxidoreductase (dehydrating) |
Comments: |
The enzyme, which has been found in rice and in members of the Apiaceae (a plant family), is a member of the 2-oxoglutarate-dependent dioxygenases, and requires ascorbate and Fe2+ for full activity. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 138263-98-6 |
References: |
1. |
Martens, S., Forkmann, G., Matern, U. and Lukačin, R. Cloning of parsley flavone synthase I. Phytochemistry 58 (2001) 43–46. [DOI] [PMID: 11524111] |
2. |
Lukačin, R., Matern, U., Junghanns, K.T., Heskamp, M.L., Britsch, L., Forkmann, G. and Martens, S. Purification and antigenicity of flavone synthase I from irradiated parsley cells. Arch. Biochem. Biophys. 393 (2001) 177–183. [DOI] [PMID: 11516175] |
3. |
Martens, S., Forkmann, G., Britsch, L., Wellmann, F., Matern, U. and Lukačin, R. Divergent evolution of flavonoid 2-oxoglutarate-dependent dioxygenases in parsley. FEBS Lett. 544 (2003) 93–98. [DOI] [PMID: 12782296] |
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[EC 1.14.20.5 created 2004 as EC 1.14.11.22, transferred 2018 to EC 1.14.20.5] |
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EC |
1.14.20.6 |
Accepted name: |
flavonol synthase |
Reaction: |
a dihydroflavonol + 2-oxoglutarate + O2 = a flavonol + succinate + CO2 + H2O |
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For diagram of flavonoid biosynthesis, click here, for diagram of kaempferol biosynthesis, click here and for diagram of myricetin biosynthesis, click here |
Other name(s): |
FLS (gene name) |
Systematic name: |
dihydroflavonol,2-oxoglutarate:oxygen oxidoreductase |
Comments: |
In addition to the desaturation of (2R,3R)-dihydroflavonols to flavonols, the enzyme from Citrus unshiu (satsuma mandarin) also has a non-specific activity that trans-hydroxylates the flavanones (2S)-naringenin and the unnatural (2R)-naringenin at C-3 to kaempferol and (2R,3R)-dihydrokaempferol, respectively [2]. Requires Fe2+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 146359-76-4 |
References: |
1. |
Wellmann, F., Lukačin, R., Moriguchi, T., Britsch, L., Schiltz, E. and Matern, U. Functional expression and mutational analysis of flavonol synthase from Citrus unshiu. Eur. J. Biochem. 269 (2002) 4134–4142. [DOI] [PMID: 12180990] |
2. |
Lukačin, R., Wellmann, F., Britsch, L., Martens, S. and Matern, U. Flavonol synthase from Citrus unshiu is a bifunctional dioxygenase. Phytochemistry 62 (2003) 287–292. [DOI] [PMID: 12620339] |
3. |
Martens, S., Forkmann, G., Britsch, L., Wellmann, F., Matern, U. and Lukačin, R. Divergent evolution of flavonoid 2-oxoglutarate-dependent dioxygenases in parsley. FEBS Lett. 544 (2003) 93–98. [DOI] [PMID: 12782296] |
4. |
Turnbull, J.J., Nakajima, J., Welford, R.W., Yamazaki, M., Saito, K. and Schofield, C.J. Mechanistic studies on three 2-oxoglutarate-dependent oxygenases of flavonoid biosynthesis: anthocyanidin synthase, flavonol synthase, and flavanone 3β-hydroxylase. J. Biol. Chem. 279 (2004) 1206–1216. [DOI] [PMID: 14570878] |
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[EC 1.14.20.6 created 2004 as EC 1.14.11.23, transferred 2018 to EC 1.14.20.6] |
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EC |
1.14.99.34 |
Accepted name: |
monoprenyl isoflavone epoxidase |
Reaction: |
7-O-methylluteone + NADPH + H+ + O2 = dihydrofurano derivatives + NADP+ + H2O |
Glossary: |
luteone = 3-(2,4-dihydroxyphenyl)-5,7-dihydroxy-6-(3-methyl-2-butenyl)-4H-1-benzopyran-4-one
naringenin = 4′,5,7-trihydroxyflavan-4-one |
Other name(s): |
monoprenyl isoflavone monooxygenase; 7-O-methylluteone:O2 oxidoreductase; 7-O-methylluteone,NADPH:O2 oxidoreductase |
Systematic name: |
7-O-methylluteone,NADPH:oxygen oxidoreductase |
Comments: |
A flavoprotein (FAD) with high specificity for monoprenyl isoflavone. The product of the prenyl epoxidation reaction contains an oxygen atom derived from O2, but not from H2O. It is slowly and non-enzymically converted into the corresponding dihydrofurano derivative. The enzyme in the fungus Botrytis cinerea is induced by the substrate analogue, 6-prenylnaringenin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 198496-86-5 |
References: |
1. |
Tanaka, M. and Tahara, S. FAD-dependent epoxidase as a key enzyme in fungal metabolism of prenylated flavonoids. Phytochemistry 46 (1997) 433–439. |
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[EC 1.14.99.34 created 2000] |
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EC |
2.1.1.46 |
Accepted name: |
isoflavone 4′-O-methyltransferase |
Reaction: |
S-adenosyl-L-methionine + a 4′-hydroxyisoflavone = S-adenosyl-L-homocysteine + a 4′-methoxyisoflavone |
|
For diagram of the biosynthesis of biochanin A, click here and for diagram of the biosynthesis of formononetin and derivatives, click here |
Other name(s): |
4′-hydroxyisoflavone methyltransferase; isoflavone methyltransferase; isoflavone O-methyltransferase |
Systematic name: |
S-adenosyl-L-methionine:4′-hydroxyisoflavone 4′-O-methyltransferase |
Comments: |
Requires Mg2+ for activity. The enzyme catalyses the methylation of daidzein and genistein. It does not methylate naringenin, apigenin, luteolin or kaempferol. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 55071-80-2 |
References: |
1. |
Wengenmayer, H., Ebel, J. and Grisebach, H. Purification and properties of a S-adenosylmethionine: isoflavone 4′-O-methyltransferase from cell suspension cultures of Cicer arietinum L. Eur. J. Biochem. 50 (1974) 135–143. [DOI] [PMID: 4452353] |
|
[EC 2.1.1.46 created 1976, modified 2011] |
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|
EC |
2.1.1.75 |
Accepted name: |
apigenin 4′-O-methyltransferase |
Reaction: |
S-adenosyl-L-methionine + apigenin = S-adenosyl-L-homocysteine + acacetin |
|
For diagram of apigenin derivatives biosynthesis, click here |
Glossary: |
apigenin = 4′,5,7-trihydroxyflavone
acacetin = 4′-methoxy-5,7-dihydroxyflavone
naringenin = 4′,5,7-trihydroxyflavan-4-one |
Other name(s): |
flavonoid O-methyltransferase; flavonoid methyltransferase; S-adenosyl-L-methionine:5,7,4′-trihydroxyflavone 4′-O-methyltransferase |
Systematic name: |
S-adenosyl-L-methionine:apigenin 4′-O-methyltransferase |
Comments: |
Converts apigenin into acacetin. Naringenin can also act as an acceptor, but more slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 118251-36-8 |
References: |
1. |
Kuroki, G. and Poulton, J.E. The para-O-methylation of apigenin to acacetin by cell-free extracts of Robinia pseudoacacia L. Z. Naturforsch. C: Biosci. 36 (1981) 916–920. |
|
[EC 2.1.1.75 created 1984] |
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EC |
2.1.1.231 |
Accepted name: |
flavonoid 4′-O-methyltransferase |
Reaction: |
S-adenosyl-L-methionine + a 4′-hydroxyflavanone = S-adenosyl-L-homocysteine + a 4′-methoxyflavanone |
|
For diagram of naringenin methyl ethers biosynthesis, click here |
Glossary: |
naringenin = 4′,5,7-trihydroxyflavan-4-one |
Other name(s): |
SOMT-2; 4′-hydroxyisoflavone methyltransferase |
Systematic name: |
S-adenosyl-L-methionine:flavonoid 4′-O-methyltransferase |
Comments: |
The enzyme catalyses the 4′-methylation of naringenin. In vitro it catalyses the 4′-methylation of apigenin, quercetin, daidzein and genistein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kim, D.H., Kim, B.G., Lee, Y., Ryu, J.Y., Lim, Y., Hur, H.G. and Ahn, J.H. Regiospecific methylation of naringenin to ponciretin by soybean O-methyltransferase expressed in Escherichia coli. J. Biotechnol. 119 (2005) 155–162. [DOI] [PMID: 15961179] |
|
[EC 2.1.1.231 created 2011] |
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EC |
2.1.1.232 |
Accepted name: |
naringenin 7-O-methyltransferase |
Reaction: |
S-adenosyl-L-methionine + (2S)-naringenin = S-adenosyl-L-homocysteine + (2S)-sakuranetin |
|
For diagram of naringenin methyl ethers biosynthesis, click here |
Glossary: |
(2S)-naringenin = (2S)-5,7,4′-trihydroxyflavan-4-one
(2S)-sakuranetin = (2S)-5,4′-dihydroxy-7-methoxyflavan-4-one |
Other name(s): |
NOMT |
Systematic name: |
S-adenosyl-L-methionine:(2S)-5,7,4′-trihydroxyflavanone 7-O-methyltransferase |
Comments: |
The enzyme is involved in the biosynthesis of the sakuranetin, an inducible defense mechanism of the plant Oryza sativa (Asian rice) against pathogen attack. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Rakwal, R., Agrawal, G.K., Yonekura, M. and Kodama, O. Naringenin 7-O-methyltransferase involved in the biosynthesis of the flavanone phytoalexin sakuranetin from rice (Oryza sativa L.). Plant Sci. 155 (2000) 213–221. [DOI] [PMID: 10814825] |
|
[EC 2.1.1.232 created 2011] |
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EC |
2.1.1.339 |
Accepted name: |
xanthohumol 4-O-methyltransferase |
Reaction: |
S-adenosyl-L-methionine + xanthohumol = S-adenosyl-L-homocysteine + 4-O-methylxanthohumol |
|
For diagram of xanthohumol biosynthesis, click here |
Glossary: |
xanthohumol = 2′,4,4′-trihydroxy-6′-methoxy-3-prenylchalcone = (2E)-1-[2,4-dihydroxy-6-methoxy-3-(3-methylbut-2-en-1-yl)phenyl]-3-(4-hydroxyphenyl)prop-2-en-1-one
4-O-methylxanthohumol =2′,4′-dihydroxy-4,6′-dimethoxy-3-prenylchalcone = (2E)-1-[2,4-dihydroxy-6-methoxy-3-(3-methylbut-2-en-1-yl)phenyl]-3-(4-methoxyphenyl)prop-2-en-1-one |
Other name(s): |
OMT2 (ambiguous); S-adenosyl-L-methionine:xanthohumol 4′-O-methyltransferase (incorrect); xanthohumol 4′-O-methyltransferase (incorrect) |
Systematic name: |
S-adenosyl-L-methionine:xanthohumol 4-O-methyltransferase |
Comments: |
The enzyme from hops (Humulus lupulus) has a broad substrate specificity. The best substrates in vitro are resveratrol, desmethylxanthohumol, naringenin chalcone and isoliquiritigenin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Nagel, J., Culley, L.K., Lu, Y., Liu, E., Matthews, P.D., Stevens, J.F. and Page, J.E. EST analysis of hop glandular trichomes identifies an O-methyltransferase that catalyzes the biosynthesis of xanthohumol. Plant Cell 20 (2008) 186–200. [DOI] [PMID: 18223037] |
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[EC 2.1.1.339 created 2017, modified 2018] |
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EC |
2.3.1.74 |
Accepted name: |
chalcone synthase |
Reaction: |
3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO2 |
|
For diagram of chalcone and stilbene biosynthesis, click here |
Glossary: |
phloretin = 3-(4-hydroxyphenyl)-1-(2,4,6-trihydroxyphenyl)propan-1-one |
Other name(s): |
naringenin-chalcone synthase; flavanone synthase; 6′-deoxychalcone synthase; chalcone synthetase; DOCS; CHS |
Systematic name: |
malonyl-CoA:4-coumaroyl-CoA malonyltransferase (cyclizing) |
Comments: |
The enzyme catalyses the first committed step in the biosynthesis of flavonoids. It can also act on dihydro-4-coumaroyl-CoA, forming phloretin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 56803-04-4 |
References: |
1. |
Ayabe, S.-I., Udagawa, A. and Furuya, T. NAD(P)H-dependent 6′-deoxychalcone synthase activity in Glycyrrhiza echinata cells induced by yeast extract. Arch. Biochem. Biophys. 261 (1988) 458–462. [DOI] [PMID: 3355160] |
2. |
Heller, W. and Hahlbrock, K. Highly purified "flavanone synthase" from parsley catalyzes the formation of naringenin chalcone. Arch. Biochem. Biophys. 200 (1980) 617–619. [DOI] [PMID: 7436427] |
3. |
Yahyaa, M., Ali, S., Davidovich-Rikanati, R., Ibdah, M., Shachtier, A., Eyal, Y., Lewinsohn, E. and Ibdah, M. Characterization of three chalcone synthase-like genes from apple (Malus x domestica Borkh.). Phytochemistry 140 (2017) 125–133. [DOI] [PMID: 28482241] |
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[EC 2.3.1.74 created 1984, modified 2018] |
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EC |
2.3.1.95 |
Accepted name: |
trihydroxystilbene synthase |
Reaction: |
3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + trans-resveratrol + 4 CO2 |
|
For diagram of chalcone and stilbene biosynthesis, click here |
Glossary: |
trans-resveratrol = 3,4′,5-trihydroxy-trans-stilbene |
Other name(s): |
resveratrol synthase; stilbene synthase (ambiguous) |
Systematic name: |
malonyl-CoA:4-coumaroyl-CoA malonyltransferase (cyclizing) |
Comments: |
Not identical with EC 2.3.1.74 naringenin-chalcone synthase or EC 2.3.1.146 pinosylvin synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 128449-70-7 |
References: |
1. |
Schöppner, A. and Kindl, H. Purification and properties of a stilbene synthase from induced cell suspension cultures of peanut. J. Biol. Chem. 259 (1984) 6806–6811. [PMID: 6427224] |
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[EC 2.3.1.95 created 1989] |
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EC
|
2.3.1.120
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Deleted entry: | 6′-deoxychalcone synthase. The reaction listed is due to EC 2.3.1.74 naringenin-chalcone synthase |
[EC 2.3.1.120 created 1990, deleted 1992] |
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EC |
2.3.1.146 |
Accepted name: |
pinosylvin synthase |
Reaction: |
3 malonyl-CoA + cinnamoyl-CoA = 4 CoA + pinosylvin + 4 CO2 |
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For diagram of chalcone and stilbene biosynthesis, click here |
Other name(s): |
stilbene synthase (ambiguous); pine stilbene synthase (ambiguous) |
Systematic name: |
malonyl-CoA:cinnamoyl-CoA malonyltransferase (cyclizing) |
Comments: |
Not identical with EC 2.3.1.74 (naringenin-chalcone synthase) or EC 2.3.1.95 (trihydroxystilbene synthase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 72994-49-1 |
References: |
1. |
Gehlert, R., Schöppner, A. and Kindl, H. Stilbene synthase from seedlings of Pinus sylvestris - purification and induction in response to fungal infection. Mol. Plant-Microbe Interaction 3 (1990) 444–449. |
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[EC 2.3.1.146 created 1992] |
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EC |
2.3.1.156 |
Accepted name: |
phloroisovalerophenone synthase |
Reaction: |
(1) isovaleryl-CoA + 3 malonyl-CoA = 4 CoA + 3 CO2 + phlorisovalerophenone (2) isobutyryl-CoA + 3 malonyl-CoA = 4 CoA + 3 CO2 + phlorisobutyrophenone |
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For diagram of polyketides biosynthesis, click here |
Glossary: |
phlorisobutyrophenone = 2-methyl-1-(2,4,6-trihydroxyphenyl)propan-1-one
phlorisovalerophenone = 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one |
Other name(s): |
valerophenone synthase; 3-methyl-1-(trihydroxyphenyl)butan-1-one synthase; acylphloroglucinol synthase; isovaleryl-CoA:malonyl-CoA acyltransferase |
Systematic name: |
acyl-CoA:malonyl-CoA acyltransferase |
Comments: |
Closely related to EC 2.3.1.74, naringenin-chalcone synthase. Also acts on isobutyryl-CoA as substrate to give phlorisobutyrophenone. The products are intermediates in the biosynthesis of the bitter acids in hops (Humulus lupulus) and glucosides in strawberry (Fragaria X ananassa). It is also able to generate naringenin chalcone from 4-coumaroyl-CoA. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Fung, S.Y., Zuurbier, K.W.M., Paniego, N.B., Scheffer, J.J.C. and Verpoorte, R. Enzymes from the biosynthesis of hop α and β acids. Proc. 26th Congr. Eur. Brew. Conv. (1997) 215–221. |
2. |
Zuurbier, K.W.M., Leser, J., Berger, T., Hofte, A.J.P., Schroder, G., Verpoorte, R. and Schroder, J. 4-Hydroxy-2-pyrone formation by chalcone and stilbene synthase with nonphysiological substrates. Phytochemistry 49 (1998) 1945–1951. [PMID: 9883590] |
3. |
Song, C., Ring, L., Hoffmann, T., Huang, F.C., Slovin, J. and Schwab, W. Acylphloroglucinol biosynthesis in strawberry fruit. Plant Physiol. 169 (2015) 1656–1670. [DOI] [PMID: 26169681] |
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[EC 2.3.1.156 created 2000] |
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EC |
2.4.1.185 |
Accepted name: |
flavanone 7-O-β-glucosyltransferase |
Reaction: |
UDP-glucose + a flavanone = UDP + a flavanone 7-O-β-D-glucoside |
|
For diagram of the biosynthesis of naringenin derivatives, click here |
Other name(s): |
uridine diphosphoglucose-flavanone 7-O-glucosyltransferase; naringenin 7-O-glucosyltransferase; hesperetin 7-O-glucosyl-transferase |
Systematic name: |
UDP-glucose:flavanone 7-O-β-D-glucosyltransferase |
Comments: |
Naringenin and hesperetin can act as acceptors. No action on flavones or flavonols. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 125752-73-0 |
References: |
1. |
McIntosh, C.A., Latchinian, L. and Mansell, R.L. Flavanone-specific 7-O-glucosyltransferase activity in Citrus paradisi seedlings: purification and characterization. Arch. Biochem. Biophys. 282 (1990) 50–57. [DOI] [PMID: 2171434] |
2. |
McIntosh, C.A. and Mansell, R.L. Biosynthesis of naringin in Citrus paradisi - UDP-glucosyl-transferase activity in grapefruit seedlings. Phytochemistry 29 (1990) 1533–1538. |
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[EC 2.4.1.185 created 1992] |
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EC |
2.4.1.236 |
Accepted name: |
flavanone 7-O-glucoside 2′′-O-β-L-rhamnosyltransferase |
Reaction: |
UDP-β-L-rhamnose + a flavanone 7-O-β-D-glucoside = UDP + a flavanone 7-O-[α-L-rhamnosyl-(1→2)-β-D-glucoside] |
|
For diagram of apigenin derivatives biosynthesis, click here, for diagram of luteolin derivatives biosynthesis, click here and for diagram of naringenin derivatives biosynthesis, click here |
Glossary: |
UDP-β-L-rhamnose = UDP-6-deoxy-β-L-mannose |
Other name(s): |
UDP-rhamnose:flavanone-7-O-glucoside-2′′-O-rhamnosyltransferase; 1→2 UDP-rhamnosyltransferase; UDP-L-rhamnose:flavanone-7-O-glucoside 2′′-O-β-L-rhamnosyltransferase |
Systematic name: |
UDP-β-L-rhamnose:flavanone-7-O-glucoside 2′′-O-α-L-rhamnosyltransferase |
Comments: |
Acts on the 7-O-glucoside of naringenin and hesperetin, also the flavone 7-O-glucosides of luteolin and apigenin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 125752-89-8 |
References: |
1. |
Bar-Peled, M., Lewinsohn, E., Fluhr, R. and Gressel, J. UDP-rhamnose:flavanone-7-O-glucoside-2′′-O-rhamnosyltransferase. Purification and characterization of an enzyme catalyzing the production of bitter compounds in citrus. J. Biol. Chem. 266 (1991) 20953–20959. [PMID: 1939145] |
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[EC 2.4.1.236 created 2004] |
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EC |
2.4.1.286 |
Accepted name: |
chalcone 4′-O-glucosyltransferase |
Reaction: |
(1) UDP-α-D-glucose + naringenin chalcone = UDP + 2′,4,4′,6′-tetrahydroxychalcone 4′-O-β-D-glucoside (2) UDP-α-D-glucose + 2′,3,4,4′,6′-pentahydroxychalcone = UDP + 2′,3,4,4′,6′-pentahydroxychalcone 4′-O-β-D-glucoside |
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For diagram of aureusidin biosynthesis, click here |
Glossary: |
naringenin chalcone = 2′,4,4′,6′-tetrahydroxychalcone = 3-(4-hydroxyphemyl)-1-(2,4,6-trihydroxyphenyl)prop-2-en-1-one
|
Other name(s): |
4′CGT |
Systematic name: |
UDP-α-D-glucose:2′,4,4′,6′-tetrahydroxychalcone 4′-O-β-D-glucosyltransferase |
Comments: |
Isolated from the plant Antirrhinum majus (snapdragon). Involved in the biosynthesis of aurones, plant flavonoids that provide yellow color to the flowers. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ono, E., Fukuchi-Mizutani, M., Nakamura, N., Fukui, Y., Yonekura-Sakakibara, K., Yamaguchi, M., Nakayama, T., Tanaka, T., Kusumi, T. and Tanaka, Y. Yellow flowers generated by expression of the aurone biosynthetic pathway. Proc. Natl. Acad. Sci. USA 103 (2006) 11075–11080. [DOI] [PMID: 16832053] |
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[EC 2.4.1.286 created 2012] |
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EC |
2.4.1.360 |
Accepted name: |
2-hydroxyflavanone C-glucosyltransferase |
Reaction: |
UDP-α-D-glucose + a 2′-hydroxy-β-oxodihydrochalcone = UDP + a 3′-(β-D-glucopyranosyl)-2′-hydroxy-β-oxodihydrochalcone |
Glossary: |
2′-hydroxy-β-oxodihydrochalcone = 1-(2-hydroxyphenyl)-3-phenypropan-1,3-dione
3′-(β-D-glucopyranosyl)-2′-hydroxy-β-oxodihydrochalcone = 1-(3-(β-D-glucopyranosyl)-2-hydroxyphenyl)-3-phenylpropan-1,3-dione |
Other name(s): |
OsCGT |
Systematic name: |
UDP-α-D-glucose:2′-hydroxy-β-oxodihydrochalcone C6/8-β-D-glucosyltransferase |
Comments: |
The enzyme has been characterized in Oryza sativa (rice), various Citrus spp., Glycine max (soybean), and Fagopyrum esculentum (buckwheat). Flavanone substrates require a 2-hydroxy group. The meta-stable flavanone substrates such as 2-hydroxynaringenin exist in an equilibrium with open forms such as 1-(4-hydroxyphenyl)-3-(2,4,6-trihydroxyphenyl)propane-1,3-dione, which are the actual substrates for the glucosyl-transfer reaction (see EC 1.14.14.162, flavanone 2-hydroxylase). The enzyme can also act on dihydrochalcones. The enzymes from citrus plants can catalyse a second C-glycosylation reaction at position 5. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Brazier-Hicks, M., Evans, K.M., Gershater, M.C., Puschmann, H., Steel, P.G. and Edwards, R. The C-glycosylation of flavonoids in cereals. J. Biol. Chem. 284 (2009) 17926–17934. [PMID: 19411659] |
2. |
Nagatomo, Y., Usui, S., Ito, T., Kato, A., Shimosaka, M. and Taguchi, G. Purification, molecular cloning and functional characterization of flavonoid C-glucosyltransferases from Fagopyrum esculentum M. (buckwheat) cotyledon. Plant J. 80 (2014) 437–448. [PMID: 25142187] |
3. |
Hirade, Y., Kotoku, N., Terasaka, K., Saijo-Hamano, Y., Fukumoto, A. and Mizukami, H. Identification and functional analysis of 2-hydroxyflavanone C-glucosyltransferase in soybean (Glycine max). FEBS Lett. 589 (2015) 1778–1786. [PMID: 25979175] |
4. |
Ito, T., Fujimoto, S., Suito, F., Shimosaka, M. and Taguchi, G. C-Glycosyltransferases catalyzing the formation of di-C-glucosyl flavonoids in citrus plants. Plant J. 91 (2017) 187–198. [DOI] [PMID: 28370711] |
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[EC 2.4.1.360 created 2018] |
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EC |
2.5.1.70 |
Accepted name: |
naringenin 8-dimethylallyltransferase |
Reaction: |
prenyl diphosphate + (–)-(2S)-naringenin = diphosphate + sophoraflavanone B |
|
For diagram of sophoraflavanone G biosynthesis, click here |
Glossary: |
dimethylallyl = prenyl = 3-methylbut-2-en-1-yl
(–)-(2S)-naringenin = (–)-(2S)-5,7-dihydroxy-2-(4-hydroxyphenyl)-2,3-dihydrochromen-4-one
sophoraflavanone B = (–)-(2S)-8-prenylnaringenin = (–)-(2S)-5,7-dihydroxy-2-(4-hydroxyphenyl)-8-(3-methylbut-2-en-1-yl)-2,3-dihydrochromen-4-one |
Other name(s): |
N8DT; dimethylallyl-diphosphate:naringenin 8-dimethylallyltransferase |
Systematic name: |
prenyl-diphosphate:naringenin 8-prenyltransferase |
Comments: |
Requires Mg2+. This membrane-bound protein is located in the plastids [2]. In addition to naringenin, the enzyme can prenylate several other flavanones at the C-8 position, but more slowly. Along with EC 1.14.14.142 (8-dimethylallylnaringenin 2′-hydroxylase) and EC 2.5.1.71 (leachianone-G 2′′-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G-biosynthesis pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Yamamoto, H., Senda, M. and Inoue, K. Flavanone 8-dimethylallyltransferase in Sophora flavescens cell suspension cultures. Phytochemistry 54 (2000) 649–655. [DOI] [PMID: 10975499] |
2. |
Zhao, P., Inoue, K., Kouno, I. and Yamamoto, H. Characterization of leachianone G 2′′-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures. Plant Physiol. 133 (2003) 1306–1313. [DOI] [PMID: 14551337] |
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[EC 2.5.1.70 created 2007] |
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EC |
2.5.1.71 |
Accepted name: |
leachianone-G 2′′-dimethylallyltransferase |
Reaction: |
prenyl diphosphate + leachianone G = diphosphate + sophoraflavanone G |
|
For diagram of sophoraflavanone G biosynthesis, click here |
Glossary: |
dimethylallyl = prenyl = 3-methylbut-2-en-1-yl
isopentenyl = 3-methylbut-3-en-1-yl
lavandulyl = 5-methyl-2-(prop-1-en-2-yl)hex-4-en-1-yl
leachianone G = (–)-(2S)-2′-hydroxy-8-prenylnaringenin = (–)-(2S)-2-(2,4-dihydroxyphenyl)-5,7-dihydroxy-8-(3-methylbut-2-en-1-yl)-2,3-dihydro-4H-chromen-4-one
sophoraflavanone G = (2S)-2-(2,4-dihydroxyphenyl)-5,7-dihydroxy-8-[(2R)-5-methyl-2-(prop-1-en-2-yl)hex-4-en-1-yl]-2,3-dihydro-4H-chromen-4-one
|
Other name(s): |
LG 2′′-dimethylallyltransferase; leachianone G 2′′-dimethylallyltransferase; LGDT; dimethylallyl-diphosphate:leachianone-G 2′′-dimethylallyltransferase |
Systematic name: |
prenyl-diphosphate:leachianone-G 2′′-prenyltransferase |
Comments: |
This membrane-bound enzyme is located in the plastids and requires Mg2+ for activity. The reaction forms the lavandulyl sidechain of sophoraflavanone G by transferring a prenyl group to the 2′′ position of another prenyl group attached at position 8 of leachianone G. The enzyme is specific for prenyl diphosphate as the prenyl donor, as it cannot be replaced by isopentenyl diphosphate or geranyl diphosphate. Euchrenone a7 (a 5-deoxy derivative of leachianone G) and kenusanone I (a 7-methoxy derivative of leachianone G) can also act as substrates, but more slowly. Along with EC 1.14.14.142 (8-dimethylallylnaringenin 2′-hydroxylase) and EC 2.5.1.70 (naringenin 8-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G-biosynthesis pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Zhao, P., Inoue, K., Kouno, I. and Yamamoto, H. Characterization of leachianone G 2′′-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures. Plant Physiol. 133 (2003) 1306–1313. [DOI] [PMID: 14551337] |
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[EC 2.5.1.71 created 2007] |
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|
EC |
2.5.1.136 |
Accepted name: |
2-acylphloroglucinol 4-prenyltransferase |
Reaction: |
prenyl diphosphate + a 2-acylphloroglucinol = diphosphate + a 2-acyl-4-prenylphloroglucinol |
|
|
Glossary: |
naringenin chalcone = 2′,4,4′,6′-tetrahydroxychalcone = 3-(4-hydroxyphenyl)-1-(2,4,6-trihydroxyphenyl)prop-2-en-1-one
phlorisovalerophenone = 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one |
Other name(s): |
PT-1 (gene name); PT1L (gene name); aromatic prenyltransferase (ambiguous); dimethylallyl-diphosphate:2-acylphloroglucinol 4-dimethylallyltransferase |
Systematic name: |
prenyl-diphosphate:2-acylphloroglucinol 4-prenyltransferase |
Comments: |
The enzyme, characterized from hop (Humulus lupulus), acts on phlorisovalerophenone, phlormethylbutanophenone, and phlorisobutanophenone during the synthesis of bitter acids. It also acts with much lower activity on naringenin chalcone. Forms a complex with EC 2.5.1.137, 2-acyl-4-prenylphloroglucinol 6-prenyltransferase, which catalyses additional prenylation reactions. Requires Mg2+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Tsurumaru, Y., Sasaki, K., Miyawaki, T., Uto, Y., Momma, T., Umemoto, N., Momose, M. and Yazaki, K. HlPT-1, a membrane-bound prenyltransferase responsible for the biosynthesis of bitter acids in hops. Biochem. Biophys. Res. Commun. 417 (2012) 393–398. [DOI] [PMID: 22166201] |
2. |
Li, H., Ban, Z., Qin, H., Ma, L., King, A.J. and Wang, G. A heteromeric membrane-bound prenyltransferase complex from hop catalyzes three sequential aromatic prenylations in the bitter acid pathway. Plant Physiol. 167 (2015) 650–659. [DOI] [PMID: 25564559] |
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[EC 2.5.1.136 created 2017] |
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